ID A0A1M7SVH2_FERGO Unreviewed; 578 AA.
AC A0A1M7SVH2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:SHN62459.1};
GN ORFNames=SAMN02745226_01291 {ECO:0000313|EMBL:SHN62459.1};
OS Fervidobacterium gondwanense DSM 13020.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=1121883 {ECO:0000313|EMBL:SHN62459.1, ECO:0000313|Proteomes:UP000184207};
RN [1] {ECO:0000313|EMBL:SHN62459.1, ECO:0000313|Proteomes:UP000184207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13020 {ECO:0000313|EMBL:SHN62459.1,
RC ECO:0000313|Proteomes:UP000184207};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FRDJ01000006; SHN62459.1; -; Genomic_DNA.
DR RefSeq; WP_072759604.1; NZ_FRDJ01000006.1.
DR AlphaFoldDB; A0A1M7SVH2; -.
DR STRING; 1121883.SAMN02745226_01291; -.
DR OrthoDB; 9769691at2; -.
DR Proteomes; UP000184207; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09610; M3B_PepF; 1.
DR Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR InterPro; IPR013647; OligopepF_N_dom.
DR InterPro; IPR042088; OligoPept_F_C.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF5; OLIGOENDOPEPTIDASE F; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF08439; Peptidase_M3_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 101..157
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 185..563
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 578 AA; 67357 MW; 01AC0FA260D24F3E CRC64;
MNWNLKEIFQ DDTAATENAK LRLNEIKKYV EEFENEQELG RLVELIKKIE DSTDNFAKSS
QYAWMRYSTD TESSESQKLI GSIQQLEAEL SESLVKMEVK LAALDDASIE KMIDLDKNYE
HKLRRIVERR KHLLSKEAEQ TLALMSVSGR GAISKIHSRL ESAYTFDIEI DGKLKTLTVE
EIKALRRSTD SHLRKRAMKM FFERFQNDSM VITEVYNLIV KNYDTESKIR RFPKPISMMN
FENEVSDEVV DKLIEVTDQY TNLVRRYYDW KSKIMGEKLT LADIYAPISA ERRIFTFDEA
KDVILESYYA FNQSAGDIVK GFFDTSRIDL LPKKGKVGGA YCIYSTTKLP PYVLTNFNGD
MYDVMTLAHE LGHGLHGTLS RKQTFFNHDT PLTLAELASV FGEFLVFDNL KNKLSKKEKM
ALLASKIEDT IATTFRQNMF TKFELRAHKK ISTDGYADWN ELNEIYHDEL KNIFGDVVEI
PEWYKNEWAM VSHFFETPFY VYAYNFAHCL VITLYQKYLE EGRTFAEKYL KLLESGGKYT
PEELLASVGI DVKEEGFWER AFRFIEHLVD ELEEAARD
//
